The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides
Open accessAbstract
Superoxide reacts rapidly with other radicals, but these reactions have received little attention in the context of oxidative stress. For tyrosyl radicals, reaction with superoxide is 3-fold faster than dimerization, and forms the addition product tyrosine hydroperoxide. We have explored structural requirements for hydroperoxide formation using tyrosine analogues and di- and tri-peptides. Superoxide and phenoxyl radicals were generated using xanthine oxidase, peroxidase and the respective tyrosine derivative, or by γ-radiation. Peroxides were measured using FeSO4/Xylenol Orange. Tyrosine and tyramine formed stable hydroperoxides, but N-acetyltyrosine and p-hydroxyphenylacetic acid did not, demonstrating a requirement for a free amino group. Using [14C]tyrosine, the hydroperoxide and dityrosine were formed at a molar ratio of 1.8:1. Studies with pre-formed hydroperoxides, and measurements of substrate losses, indicated that, in the absence of a free amino group, reaction with superoxide resulted primarily in restitution of the parent compound. With dipeptides, hydroperoxides were formed only on N-terminal tyrosines. However, adjacent lysines promoted hydroperoxide formation, as did addition of free lysine or ethanolamine. Results are compatible with a mechanism [d'Alessandro, Bianchi, Fang, Jin, Schuchmann and von Sonntag (2000) J. Chem. Soc. Perkin Trans. II, 1862–1867] in which the phenoxyl radicals react initially with superoxide by addition, and the intermediate formed either releases oxygen to regenerate the parent compound or is converted into a hydroperoxide. Amino groups favour hydroperoxide formation through Michael addition to the tyrosyl ring. These studies indicate that tyrosyl hydroperoxides should be formed in proteins where there is a basic molecular environment. The contribution of these radical reactions to oxidative stress warrants further investigation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“For tyrosyl radicals, the reaction with superoxide to form the addition product (tyrosine hydroperoxide) is three times faster than dimerization [139,141].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [139]
In the citing paper
“The hydroperoxide, due to the resonant forms of Tyr, can be formed in the ortho or para position with respect to the phenoxyl radical [138,139,140], Figure 51 and Figure 52.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [139]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
A SPECTROPHOTOMETRIC METHOD FOR MEASURING THE BREAKDOWN OF HYDROGEN PEROXIDE BY CATALASE
Beers, R. F., & Sizer, I. W. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50881-x · Cited by 6,781
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513
Free Radicals in Biology and Medicine
Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871
Biochemistry and pathology of radical-mediated protein oxidation
Dean, R. T., Fu, S., Stocker, R., & Davies, M. J. (1997) · Biochemical Journal · doi:10.1042/bj3240001 · Cited by 1,678
Self-citationWolff, S. P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33021-2 · Cited by 1,240
Photo-oxidation of proteins and its role in cataractogenesis
Davies, M. J., & Truscott, R. J. W. (2001) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(01)00208-1 · Cited by 446
Self-citationSuperoxide as an intracellular radical sink
Winterbourn, C. C. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90512-s · Cited by 364
Self-citationTyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.
Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354
Formation of peroxides in amino acids and proteins exposed to oxygen free radicals
Gebicki, S., & Gebicki, J. M. (1993) · Biochemical Journal · doi:10.1042/bj2890743 · Cited by 305
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Protein oxidation and peroxidation
Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952
Self-citationPeroxynitrite, a Stealthy Biological Oxidant
Radí, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.472936 · Cited by 929
Hoye, A. T., Davoren, J. E., Wipf, P., Fink, M. P., & Kagan, V. E. (2008) · Accounts of Chemical Research · doi:10.1021/ar700135m · Cited by 643
Stress-induced reactive oxygen species compartmentalization, perception and signalling
Castro, B., Citterico, M., Kimura, S., Stevens, D. M., Wrzaczek, M., & Coaker, G. (2021) · Nature Plants · doi:10.1038/s41477-021-00887-0 · Cited by 462
Photodynamic Therapy: Current Status and Future Directions
Benov, L. (2014) · Medical Principles and Practice · doi:10.1159/000362416 · Cited by 438
Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
Davies, M. J. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.11-006fr · Cited by 412
Self-citationSuperoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342
Mitochondria-targeted peptide antioxidants: Novel neuroprotective agents
Szeto, H. H. (2006) · The AAPS Journal · doi:10.1208/aapsj080362 · Cited by 332
Cell-permeable, mitochondrial-targeted, peptide antioxidants
Szeto, H. H. (2006) · The AAPS Journal · doi:10.1007/bf02854898 · Cited by 316
Mitochondria-Targeted Cytoprotective Peptides for Ischemia–Reperfusion Injury
Szeto, H. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1892 · Cited by 274
Powers, S. K., Hudson, M. B., Nelson, W. B., Talbert, E. E., Min, K., Szeto, H. H., Kavazis, A. N., & Smuder, A. J. (2011) · Critical Care Medicine · doi:10.1097/ccm.0b013e3182190b62 · Cited by 255
Mitochondrial Dysfunction in Aging and Alzheimer's Disease: Strategies to Protect Neurons
Reddy, P. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1754 · Cited by 188
Mechanisms of catalase activity of heme peroxidases
Vlasits, J., Jakopitsch, C., Bernroitner, M., Zámocký, M., Furtmüller, P. G., & Obinger, C. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.04.018 · Cited by 182
Mitochondria as a target in treatment
Frantz, M., & Wipf, P. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20554 · Cited by 183
Cho, S., Szeto, H. H., Kim, E., Kim, H., Tolhurst, A. T., & Pinto, J. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609388200 · Cited by 170
Novel Therapies Targeting Inner Mitochondrial Membrane—From Discovery to Clinical Development
Szeto, H. H., & Schiller, P. W. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0476-8 · Cited by 175
Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite
Carballal, S., Bartesaghi, S., & Radí, R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.005 · Cited by 162
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 161
Urate as a Physiological Substrate for Myeloperoxidase
Meotti, F. C., Jameson, G. N. L., Turner, R., Harwood, D. T., Stockwell, S., Rees, M. D., Thomas, S. R., & Kettle, A. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172460 · Cited by 133
Bilirubin Links Heme Metabolism to Neuroprotection by Scavenging Superoxide
Vasavda, C., Kothari, R., Malla, A. P., Tokhunts, R. A., Lin, A. L., Ji, M., Ricco, C., Xu, R., Saavedra, H. G., Sbodio, J. I., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.07.006 · Cited by 129
Mitochondria‐Targeted Antioxidants: Future Perspectives in Kidney Ischemia Reperfusion Injury
Kezić, A., Spasojević, I., Ležaić, V., & Bajčetić, M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2950503 · Cited by 135
Houée-Lévin, C., Bobrowski, K., Horakova, L., Karademir, B., Schöneich, C., Davies, M. J., & Spickett, C. M. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1007968 · Cited by 126
Self-citationMitchell, W., Ng, E. A., Tamucci, J. D., Boyd, K. J., Sathappa, M., Coscia, A., Pan, M., Han, X., Eddy, N. A., May, E. R., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012094 · Cited by 133
Grassi, L., & Cabrele, C. (2019) · Amino Acids · doi:10.1007/s00726-019-02787-2 · Cited by 100
Suárez, J., Ranguelova, K., Jarzęcki, A. A., Manzerova, J., Krymov, V., Zhao, X., Yu, S., Metlitsky, L., Gerfen, G. J., & Magliozzo, R. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808106200 · Cited by 98
Fuentes-Lemus, E., Hägglund, P., López‐Alarcón, C., & Davies, M. J. (2021) · Molecules · doi:10.3390/molecules27010015 · Cited by 100
Self-citationBiological chemistry of superoxide radicals
Winterbourn, C. C. (2020) · ChemTexts · doi:10.1007/s40828-019-0101-8 · Cited by 100
Self-citationPari, R. F., Uju, U., Hardiningtyas, S. D., Ramadhan, W., Wakabayashi, R., Goto, M., & Kamiya, N. (2025) · Marine Drugs · doi:10.3390/md23020056 · Cited by 95
Campolo, N., Issoglio, F. M., Estrin, D. A., Bartesaghi, S., & Radí, R. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190052 · Cited by 84
Villamena, F. A., Xia, S., Merle, J. K., Lauricella, R., Tuccio, B., Hadad, C. M., & Zweier, J. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0702622 · Cited by 79
Villamena, F. A., Das, A. K., & Nash, K. M. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.74 · Cited by 85
Kudin, A. P., Dębska–Vielhaber, G., & Kunz, W. S. (2005) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2005.03.012 · Cited by 76
Real-time Measurements of Amino Acid and Protein Hydroperoxides Using Coumarin Boronic Acid
Michalski, R., Zielonka, J., Gapys, E., Marcinek, A., Joseph, J., & Kalyanaraman, B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.553727 · Cited by 75
Medical Applications of Rose Bengal‐ and Riboflavin‐Photosensitized Protein Crosslinking
Redmond, R. W., & Kochevar, I. E. (2019) · Photochemistry and Photobiology · doi:10.1111/php.13126 · Cited by 72
Mitochondrial-targeted penetrating peptide delivery for cancer therapy
Wu, J., Li, J., Wang, H., & Liu, C.-B. (2018) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2018.1517750 · Cited by 67
Chen, Y., Zhang, X., & Feng, S. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.8b00890 · Cited by 65
Identification and characterization of protein cross-links induced by oxidative reactions
Hägglund, P., Mariotti, M., & Davies, M. J. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1509710 · Cited by 61
Self-citationHypobromous acid and bromamine production by neutrophils and modulation by superoxide
Chapman, A., Skaff, O., Senthilmohan, R., Kettle, A. J., & Davies, M. J. (2008) · Biochemical Journal · doi:10.1042/bj20071563 · Cited by 57
Self-citationThe polymerization of melanin: a poorly understood phenomenon with egregious biological implications
Sarangarajan, R., & Apte, S. (2006) · Melanoma Research · doi:10.1097/01.cmr.0000195699.35143.df · Cited by 55
Bayati, M., & Poojary, M. M. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.142208 · Cited by 52
Bruno, G., Wenske, S., Lackmann, J., Lalk, M., von Woedtke, T., & Wende, K. (2020) · Biomolecules · doi:10.3390/biom10121687 · Cited by 54
Kim, S.-U., Liu, Y., Nash, K. M., Zweier, J. L., Rockenbauer, A., & Villamena, F. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105198c · Cited by 54
Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809396200 · Cited by 53
Self-citationMöller, M. N., Hatch, D. M., Kim, H.-Y. H., & Porter, N. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307215z · Cited by 50
Oxidation as an important factor of protein damage: Implications for Maillard reaction
Trnková, L., Dršata, J., & Boušová, I. (2015) · Journal of Biosciences · doi:10.1007/s12038-015-9523-7 · Cited by 52
Carroll, L., Pattison, D. I., Davies, J. B., Anderson, R. F., Lopez-Alarcon, C., & Davies, M. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.033 · Cited by 48
Self-citationFuentes-Lemus, E., Silva, E., Leinisch, F., Dorta, E., Lorentzen, L. G., Davies, M. J., & López‐Alarcón, C. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.02.090 · Cited by 47
Self-citationReactions of Superoxide with Myeloperoxidase and Its Products
Winterbourn, C. C., & Kettle, A. J. (2004) · Japanese Journal of Infectious Diseases · doi:10.7883/yoken.jjid.2004.s31 · Cited by 42
Self-citationMariotti, M., Leinisch, F., Leeming, D. J., Svensson, B., Davies, M. J., & Hägglund, P. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00881 · Cited by 38
Self-citationProton Conduction in a Tyrosine‐Rich Peptide/Manganese Oxide Hybrid Nanofilm
Lee, J., Choe, I. R., Kim, Y., Namgung, S. D., Jin, K., Ahn, H., Sung, T., Kwon, J., Lee, Y., & Nam, K. T. (2017) · Advanced Functional Materials · doi:10.1002/adfm.201702185 · Cited by 37
Patrício, E. D. S., Prado, F. M., da Silva, R. P., Carvalho, L. A. D. C., Prates, M. V. C., Dadamos, T. R. L., Bertotti, M., Mascio, P. D., Kettle, A. J., & Meotti, F. C. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00132 · Cited by 35
Reactions of superoxide with the myoglobin tyrosyl radical
Das, A. B., Nagy, P., Abbott, H. F., Winterbourn, C. C., & Kettle, A. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.039 · Cited by 34
Self-citationDavies, M. J. (2012) · Wiley eBooks · doi:10.1002/9781119953678.rad045 · Cited by 38
Self-citationKameda, T., Ohkawa, R., Yano, K., Usami, Y., Miyazaki, A., Matsuda, K., Kawasaki, K., Sugano, M., Kubota, T., & Tozuka, M. (2015) · Journal of Lipids · doi:10.1155/2015/592594 · Cited by 33
Das, A. B., Nauser, T., Koppenol, W. H., Kettle, A. J., Winterbourn, C. C., & Nagy, P. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.006 · Cited by 33
Self-citationLeinisch, F., Mariotti, M., Hägglund, P., & Davies, M. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.008 · Cited by 32
Self-citationRibose sugars generate internal glycation cross-links in horse heart myoglobin
Bokiej, M., Livermore, A. T., Harris, A. W., Onishi, A. C., & Sandwick, R. K. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.02.138 · Cited by 31
Ferreira, L. F., Moylan, J. S., Stasko, S. A., Smith, J. D., Campbell, K. S., & Reid, M. B. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01269.2011 · Cited by 31
van Dalen, C. J., Winterbourn, C. C., & Kettle, A. J. (2006) · Biochemical Journal · doi:10.1042/bj20051470 · Cited by 33
Self-citationVillamena, F. A. (2013) · Wiley eBooks · doi:10.1002/9781118355886.ch1 · Cited by 31
Superoxide radical anions protect enkephalin from oxidation if the amine group is blocked
Mozziconacci, O., Mirkowski, J., Rusconi, F., Pernot, P., Bobrowski, K., & Houée‐Levin, C. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.04.006 · Cited by 29
Clausen, M. R., Huvaere, K., Skibsted, L. H., & Stagsted, J. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903470p · Cited by 27
Prokaryotic Collagen-Like Proteins as Novel Biomaterials
Picker, J., Lan, Z., Arora, S., Green, M., Hahn, M. S., Cosgriff‐Hernandez, E., & Höök, M. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.840939 · Cited by 26
Conjugation of Glutathione to Oxidized Tyrosine Residues in Peptides and Proteins
Nagy, P., Lechte, T. P., Das, A. B., & Winterbourn, C. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371690 · Cited by 26
Self-citationPeroxides in Biological Systems
Cadet, J., & Mascio, P. D. (2009) · Patai's chemistry of functional groups · doi:10.1002/9780470682531.pat0357 · Cited by 27
Arsenate and arsenite differential toxicity in Tetrahymena thermophila
Rodríguez-Martín, D., Murciano, A., Herráiz, M., de Francisco, P., Amaro, F., Gutiérrez, J. C., Martín‐González, A., & Díaz, S. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.128532 · Cited by 25
Cell-permeable, Mitochondrial-targeted, Peptide Antioxidants
Szeto, H. (2006) · The AAPS Journal · doi:10.1208/aapsj080232 · Cited by 25
Neutrophil-mediated oxidation of enkephalins via myeloperoxidase-dependent addition of superoxide
Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.033 · Cited by 24
Self-citationOxidative inactivation of protein tyrosine phosphatase 1B by organic hydroperoxides
Bhattacharya, S., LaButti, J. N., Seiner, D. R., & Gates, K. S. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.029 · Cited by 25
Biological Chemistry of Reactive Oxygen Species
Winterbourn, C. C. (2012) · Wiley eBooks · doi:10.1002/9781119953678.rad077 · Cited by 22
Self-citationDeviers, J., Cailliez, F., de la Lande, A., & Kattnig, D. R. (2021) · The Journal of Chemical Physics · doi:10.1063/5.0078115 · Cited by 20
Redox regulation in lifespan determination
Karagianni, C., & Bazopoulou, D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105761 · Cited by 26
Superoxide dismutase protects ribonucleotide reductase from inactivation in yeast
Das, A. B., Sadowska‐Bartosz, I., Königstorfer, A., Kettle, A. J., & Winterbourn, C. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.001 · Cited by 20
Self-citationMishra, A., Lelieveld, S., Pöschl, U., & Berkemeier, T. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c03556 · Cited by 19
Stoichevska, V., An, B., Peng, Y. Y., Yiğit, S., Vashi, A. V., Kaplan, D. L., Werkmeister, J. A., Dumsday, G. J., & Ramshaw, J. A. M. (2016) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.35772 · Cited by 15
Li, M., Kong, D., Meng, L., Wang, Z., Bai, Z., & Wu, G. (2024) · RSC Advances · doi:10.1039/d4ra05517a · Cited by 14
Protein-encapsulated bilirubin: paving the way to a useful probe for singlet oxygen
Pimenta, F. M., Jensen, J. K., Etzerodt, M., & Ogilby, P. R. (2014) · Photochemical & Photobiological Sciences · doi:10.1039/c4pp00408f · Cited by 13
Folkes, L. K., Bartesaghi, S., Trujillo, M., Wardman, P., & Radí, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031797 · Cited by 13
Skjoldager, N., Bang, M. B., Rykær, M., Björnberg, O., Davies, M. J., Svensson, B., Harris, P., & Hägglund, P. (2017) · Scientific Reports · doi:10.1038/srep46282 · Cited by 12
Self-citationRodacka, A. (2015) · International Journal of Radiation Biology · doi:10.3109/09553002.2015.1106022 · Cited by 11
Reactivity of mitochondrial peroxiredoxins with biological hydroperoxides
Trujillo, M., Piacenza, L., & Radí, R. (2023) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2023.100017 · Cited by 10
Field, S. M., & Villamena, F. A. (2008) · Chemical Research in Toxicology · doi:10.1021/tx8001687 · Cited by 10
Gatin, A., Duchambon, P., van der Rest, G., Billault, I., & Sicard‐Roselli, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031174 · Cited by 8
Epidermal hydrogen peroxide is not increased in lesional and non-lesional skin of vitiligo
Zailaie, M. Z. (2016) · Archives of Dermatological Research · doi:10.1007/s00403-016-1695-y · Cited by 7
Mitchell, W., Ng, E. A., Tamucci, J. D., Boyd, K., Sathappa, M., Coscia, A., Pan, M., Han, X., Eddy, N. A., May, E. R., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/735001 · Cited by 7
Vo, Q. V., Hang, D. T. N., Hòa, N. T., Nam, P. C., Duong, T. Q., & Mechler, Á. (2023) · New Journal of Chemistry · doi:10.1039/d3nj01800h · Cited by 6
Zhou, Q., Zhang, X., & Zhou, C. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.125662 · Cited by 6
Chen, T., Liou, S.-Y., Wu, H., Tsai, F., Tsai, C., Huang, C., & Chang, Y.-L. (2010) · International Urology and Nephrology · doi:10.1007/s11255-010-9722-y · Cited by 6
Muñoz‐Rugeles, L., Galano, A., & Alvarez-Idaboy, J. R. (2020) · New Journal of Chemistry · doi:10.1039/c9nj04998c · Cited by 5
Jørgensen, S. M., Lorentzen, L. G., Hammer, A., Höefler, G., Malle, E., Chuang, C. Y., & Davies, M. J. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102794 · Cited by 6
Self-citationFolkes, L. K., Bartesaghi, S., Trujillo, M., Wardman, P., & Radí, R. (2021) · Free Radical Research · doi:10.1080/10715762.2020.1870684 · Cited by 5
Selective Protection of Normal Cells during Chemotherapy by RY4 Peptides
Wu, X., Liu, L., Zhang, Z.-F., Zhang, B., Sun, H., Chan, G. L., & Li, N. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0425 · Cited by 5
Ondrasik, R. M., Chen, Q., Navitsky, K., Chau, W. L., Devine, I., Lau, O., Galbreath, T., Barsotti, R., & Young, L. H. (2013) · American Peptide Symposium (APS) · doi:10.17952/23aps.2013.064 · Cited by 4
Hydroxylation of 3-Nitrotyrosine and Its Derivatives by Gamma Irradiation
Shi, W., Dong, J.-C., Zhao, Y., & Li, Y. (2006) · Radiation Research · doi:10.1667/rr0612.1 · Cited by 4
Oxidative degradation of surfactants: mechanisms
Schöneich, C. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-812503-8.00006-3 · Cited by 3
Oxidative stress in neurodegeneration: targeting mitochondria as a therapeutic aid
Gaggelli, E., & Valensin, G. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_12 · Cited by 3
Cell-Permeable, Mitochondrial-Targeted, Peptide Antioxidants
Szeto, H. H. (2008) · Springer eBooks · doi:10.1007/978-0-387-76678-2_31 · Cited by 4
Oxygenation is the main pathway for the reaction between superoxide anion and tryptophan radical
Zhuravleva, Y. S., & Sherin, P. S. (2025) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2025.116571 · Cited by 2
Schöneich, C. (2015) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-1-4939-2543-8_9 · Cited by 2
Billault, I., Gatin, A., van der Rest, G., & Sicard‐Roselli, C. (2022) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03782-x · Cited by 2
Metadata
- Authors
- WINTERBOURN, C. C., PARSONS-MAIR, H. N., GEBICKI, S., GEBICKI, J. M., & DAVIES, M. J.
- Affiliations
- Department of Pathology, Christchurch School of Medicine and Health Sciences, P.O. Box 4345, Christchurch, New Zealand
- Macquarie University (AU)
- The Heart Research Institute (AU)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2004-06-22
- Volume
- 381
- Issue
- 1
- Pages
- 241-248
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1133782
- OpenAlex
- W1970577924
- Cited by
- 112
- References
- 48
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 3 · 2023: 6 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 7 · 2018: 9 · 2017: 3 · 2016: 5 · 2015: 6 · 2014: 6 · 2013: 4 · 2012: 7
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- superoxide, tyrosyl radical, phenoxyl radicals, oxidative stress, tyrosine analogues, dipeptides, tripeptides, free amino groups, Michael addition, dityrosine, lysine, tyramine, N-acetyltyrosine, p-hydroxyphenylacetic acid, radical addition, protein oxidation
- MeSH terms
- Amines, Free Radicals, Hydrogen Peroxide, Models, Chemical, Peptides, Superoxides, Tyrosine, Dimerization
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review